PLB5_SCHPO
ID PLB5_SCHPO Reviewed; 623 AA.
AC Q9Y7N6;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Putative lysophospholipase C1450.09c;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B;
DE Flags: Precursor;
GN ORFNames=SPCC1450.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; CU329672; CAB40176.3; -; Genomic_DNA.
DR PIR; T40991; T40991.
DR RefSeq; NP_588308.2; NM_001023298.3.
DR AlphaFoldDB; Q9Y7N6; -.
DR SMR; Q9Y7N6; -.
DR BioGRID; 275706; 33.
DR STRING; 4896.SPCC1450.09c.1; -.
DR PaxDb; Q9Y7N6; -.
DR PRIDE; Q9Y7N6; -.
DR EnsemblFungi; SPCC1450.09c.1; SPCC1450.09c.1:pep; SPCC1450.09c.
DR PomBase; SPCC1450.09c; -.
DR VEuPathDB; FungiDB:SPCC1450.09c; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q9Y7N6; -.
DR OMA; SRHFANG; -.
DR PhylomeDB; Q9Y7N6; -.
DR Reactome; R-SPO-111995; phospho-PLA2 pathway.
DR Reactome; R-SPO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-SPO-1482798; Acyl chain remodeling of CL.
DR Reactome; R-SPO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-SPO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-SPO-1482922; Acyl chain remodelling of PI.
DR Reactome; R-SPO-1482925; Acyl chain remodelling of PG.
DR Reactome; R-SPO-1483115; Hydrolysis of LPC.
DR Reactome; R-SPO-1483152; Hydrolysis of LPE.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR Reactome; R-SPO-2142753; Arachidonic acid metabolism.
DR Reactome; R-SPO-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-SPO-432142; Platelet sensitization by LDL.
DR Reactome; R-SPO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9Y7N6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IC:PomBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; ISS:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..623
FT /note="Putative lysophospholipase C1450.09c"
FT /id="PRO_0000024643"
FT DOMAIN 67..607
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 623 AA; 67043 MW; 7180BF849DBF0A69 CRC64;
MKLSSFGLFL ALQLLPALGL PSRIDEVDVS DPELIGLLKP DNVDKPANSI PLSKRSTSPS
YAPYTVACPS GSLLRPASDG LSTGEQEFVD KRVSKVNSAL ESFISKTGLK IDTKSVLNDT
DGPRLGIAIS GGGFPAMLTG AGAINAFDAR NGNTTSLGGI LQSSMYLTGL SGGSWLVGSV
AVNNFANITF LHDDVWNLDH SLFAPYDDAF ENFYIYQEWF EQVLQKKNAG FNVSITDLWG
RALALKLVNP LTGGANTTFS SVTNETWFQD GEFPFPIIIA DNVIEGETVI PLNDTVFEFT
PIEFGTWDTG VESFIPMEYT GTHLINGIPL NESCVRNFDN AGFLMGTSSN VFSGILPATN
ASLTASNNTF NNAVLSFLEM LAEDQLDVGL YPNPYQGYGN ASNTTTTNPL EPYPIIELID
GGSDSEGIPF WPLLHPQRDV DVIFAIDGGY QSATSGWPDG SSLVSTYERV LATNSSGVRG
FPYIPDTNTF LALGLNTHPT FFGCDGRNTT AGNHTVNDDT PPLVVYFPNY PWTMYANVTT
YTVQLEDTLS SGMIENAAVA ATQNNSDSFA VCVACALVQR SLERKNMSTP SQCASCFNQY
CWNGTIASTT VTTYAPTVLS AKI
